Evidence map›Paper›PMID 32134144›Full record

ArticleThe EMBO journal2020

Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1.

Bethan Medina-Pritchard, Vasiliki Lazou, Juan Zou, Olwyn Byron, Maria A Abad, Juri Rappsilber, Patrick Heun, A Arockia Jeyaprakash

Abstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Retention of a singlebioRxiv : the preprint server for biology · 2025
    Article
  6. Centromere regulation in the germline and early embryo.Current opinion in genetics & development · 2025
    Review
  7. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. The N-terminal tail ofMolecular biology of the cell · 2021
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Bethan Medina-PritchardWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.ORCID 0000-0002-6736-9203
Vasiliki LazouWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Juan ZouWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Olwyn ByronSchool of Life Sciences, University of Glasgow, Glasgow, UK.
Maria A AbadWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Juri RappsilberWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.ORCID 0000-0001-5999-1310
Patrick HeunWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
A Arockia JeyaprakashWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.ORCID 0000-0002-1889-8635

Funding

European Research Council Starting-Consolidator Grant 311674Multi-User Equipment grant 101527/Z/13/ZWellcome Trust 084229Wellcome Trust 091020Wellcome Trust 092076Wellcome Trust 095822Wellcome Trust 103897Wellcome Trust 202811Wellcome Trust 202811/Z/16/ZWellcome Trust 203149
6 · The paper itself

Abstract

Centromeres are microtubule attachment sites on chromosomes defined by the enrichment of histone variant CENP-A-containing nucleosomes. To preserve centromere identity, CENP-A must be escorted to centromeres by a CENP-A-specific chaperone for deposition. Despite this essential requirement, many eukaryotes differ in the composition of players involved in centromere maintenance, highlighting the plasticity of this process. In humans, CENP-A recognition and centromere targeting are achieved by HJURP and the Mis18 complex, respectively. Using X-ray crystallography, we here show how Drosophila CAL1, an evolutionarily distinct CENP-A histone chaperone, binds both CENP-A and the centromere receptor CENP-C without the requirement for the Mis18 complex. While an N-terminal CAL1 fragment wraps around CENP-A/H4 through multiple physical contacts, a C-terminal CAL1 fragment directly binds a CENP-C cupin domain dimer. Although divergent at the primary structure level, CAL1 thus binds CENP-A/H4 using evolutionarily conserved and adaptive structural principles. The CAL1 binding site on CENP-C is strategically positioned near the cupin dimerisation interface, restricting binding to just one CAL1 molecule per CENP-C dimer. Overall, by demonstrating how CAL1 binds CENP-A/H4 and CENP-C, we provide key insights into the minimalistic principles underlying centromere maintenance.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCentromereCentromere Protein AChromosomal Proteins, Non-HistoneCrystallography, X-RayDrosophilaDrosophila ProteinsHydrophobic and Hydrophilic InteractionsModels, MolecularMutationProtein BindingCal1 protein, DrosophilaCENP-C protein, DrosophilaCentromere Protein AChromosomal Proteins, Non-HistoneCid protein, DrosophilaDrosophila ProteinsCAL1CENP-ACENP-Ccentromereschromosome segregation

Identifiers

PMID32134144
PMCPMC7110144

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.